Fluorescence Quantum Yield of Thioflavin T in Rigid Isotropic Solution and Incorporated into the Amyloid Fibrils

被引:149
作者
Sulatskaya, Anna I. [1 ]
Maskevich, Alexander A. [2 ]
Kuznetsova, Irina M. [1 ]
Uversky, Vladimir N. [3 ,4 ]
Turoverov, Konstantin K. [1 ]
机构
[1] Russian Acad Sci, Inst Cytol, St Petersburg 194064, Russia
[2] Yanka Kupala Grodno State Univ, Grodno, BELARUS
[3] Russian Acad Sci, Inst Biol Instrumentat, Pushchino 142292, Russia
[4] Indiana Univ Sch Med, Dept Biochem & Mol Biol, Indianapolis, IN USA
来源
PLOS ONE | 2010年 / 5卷 / 10期
关键词
TORSIONAL RELAXATION; BINDING-SITES; PROTEIN; DISEASE; AGGREGATION; PEPTIDES; SOLVENTS; KINETICS; INSULIN; DYE;
D O I
10.1371/journal.pone.0015385
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
In this work, the fluorescence of thioflavin T (ThT) was studied in a wide range of viscosity and temperature. It was shown that ThT fluorescence quantum yield varies from 0.0001 in water at room temperature to 0.28 in rigid isotropic solution (T/eta -> 0). The deviation of the fluorescence quantum yield from unity in rigid isotropic solution suggests that fluorescence quantum yield depends not only on the ultra-fast oscillation of ThT fragments relative to each other in an excited state as was suggested earlier, but also depends on the molecular configuration in the ground state. This means that the fluorescence quantum yield of the dye incorporated into amyloid fibrils must depend on its conformation, which, in turn, depends on the ThT environment. Therefore, the fluorescence quantum yield of ThT incorporated into amyloid fibrils can differ from that in the rigid isotropic solution. In particular, the fluorescence quantum yield of ThT incorporated into insulin fibrils was determined to be 0.43. Consequently, the ThT fluorescence quantum yield could be used to characterize the peculiarities of the fibrillar structure, which opens some new possibilities in the ThT use for structural characterization of the amyloid fibrils.
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页数:7
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